Calcitonin, porcine is a highly purified, 32-amino acid polypeptide hormone naturally synthesized by the thyroid C-cells of pigs, supplied as a sterile lyophilized white powder for advanced endocrinological and osteological research. Structurally characterized by a disulfide bridge between Cys1 and Cys7 and a C-terminal proline amide, this peptide shares high sequence homology with human calcitonin, making it a vital tool for scientists studying calcium homeostasis, bone metabolism, and G-protein-coupled receptor (GPCR) signaling. Its well-defined conformation and specific biological activity make it an essential reference standard for pharmaceutical R&D, biochemical laboratories, and academic institutions focused on antiresorptive drug discovery, hypercalcemia mechanisms, and the comparative physiology of calcitonin receptors across mammalian species.
Antho-RFamide is a high-purity, synthetic pentapeptide neuropeptide (pGlu-Gly-Arg-Phe-NH2) originally isolated from marine cnidarians such as the sea anemone Anthopleura elegantissimaand the sea pansy Renilla köllikeri, supplied as a lyophilized white powder for advanced neurobiological and evolutionary research. As a canonical member of the RFamide family of neuropeptides, it features a signature C-terminal Arg-Phe-NH2 (RFamide) motif and an N-terminal pyroglutamate residue, making it a fundamental tool for scientists studying primitive nervous systems, neuromuscular junctions, and G-protein-coupled receptor (GPCR) signaling. Its well-defined sequence and potent bioactivity make it an essential reference standard for academic laboratories, marine biology institutes, and pharmaceutical R&D teams focused on neurophysiology, comparative neuroscience, and the exploration of novel GPCR ligands derived from marine organisms.
CTX IV (6-12) is a synthetic peptide fragment corresponding to the C-terminal telopeptide region of type I collagen, specifically cleaved by the enzyme cathepsin K during bone resorption. This high-purity peptide serves as a critical reference standard for researchers studying bone turnover, osteoporosis, and other metabolic bone diseases, offering reliable calibration for ELISA and mass spectrometry assays.
β-Amyloid (1-34) is a synthetic peptide fragment representing the N-terminal region of the full-length β-amyloid protein, which is critically involved in the pathogenesis of Alzheimer’s disease. This peptide is widely used in neuroscience research to study amyloid aggregation, neurotoxicity, and early-stage plaque formation, offering researchers a valuable tool to investigate disease mechanisms and potential therapeutic targets in both academic and pharmaceutical settings.
ACTH (18-39) (human) is a synthetic peptide fragment derived from the C-terminal region of adrenocorticotropic hormone (ACTH), retaining full biological activity for stimulating adrenal glucocorticoid production. This peptide is widely used in endocrinology and metabolic research to investigate adrenal cortex function, steroidogenesis regulation, and hypothalamic-pituitary-adrenal (HPA) axis dynamics. Its high purity and stability make it suitable for in vitro cellular assays and in vivo animal models studying stress response, inflammation modulation, and energy homeostasis.
Amylin (20-29) (human) is a synthetic peptide corresponding to the C-terminal decapeptide of human amylin, a hormone co-secreted with insulin by pancreatic beta-cells. This peptide plays a crucial role in regulating postprandial glucose homeostasis by modulating gastric emptying, suppressing glucagon secretion, and promoting satiety. It is widely used as a research tool to study islet function, diabetes pathogenesis, and the physiological interplay between amylin and insulin in metabolic control.
Met-Lys-Bradykinin, also known as Methionyl-Lysyl-Bradykinin or MK-Bradykinin, is a synthetic undecapeptide and a structurally defined analog of the endogenous vasoactive hormone Bradykinin, supplied as a high-purity lyophilized powder for specialized pharmacological and biochemical research. This peptide features an N-terminal extension of methionine and lysine residues attached to the Bradykinin sequence, making it a vital tool for scientists investigating the kallikrein-kinin system, G-protein-coupled receptor (GPCR) signaling, and peptide metabolism. Its well-characterized properties and specific receptor interactions make it an essential reference standard for pharmaceutical R&D, academic laboratories, and biotechnology firms focused on cardiovascular physiology, inflammatory pathways, nociception, and the development of novel kinin-based therapeutics.
Lys-(Ala3)-Bradykinin, also referred to as KR-10, is a synthetic decapeptide analog of the endogenous vasoactive hormone Bradykinin, featuring a specific N-terminal lysine extension and a proline-to-alanine substitution at the third position, supplied as a high-purity lyophilized white powder for advanced pharmacological research. This structurally modified peptide serves as a critical tool for scientists investigating the kallikrein-kinin system, offering altered receptor binding dynamics and enhanced metabolic stability compared to the native nonapeptide. Its well-defined sequence and unique conformational properties make it an essential reference standard for pharmaceutical R&D, biochemical laboratories, and academic institutions focused on cardiovascular physiology, inflammatory signaling pathways, nociception, and the structure-activity relationship studies of G-protein-coupled receptor ligands.
Defensin HNP-2 (human) is a cationic antimicrobial peptide predominantly found in human neutrophils, playing a vital role in the innate immune response against invading pathogens. This peptide exhibits high specificity for disrupting microbial membranes and is widely utilized in immunological and microbiological research to explore host defense mechanisms and inflammatory responses.
Angiotensin A, also widely recognized in the scientific community as Angiotensin I or Angiotensin-(1-10), is a highly purified decapeptide hormone supplied as a lyophilized white powder, serving as the essential precursor substrate within the Renin-Angiotensin System (RAS). This research-grade peptide is a fundamental tool for pharmacologists, biochemists, and cardiovascular researchers investigating blood pressure regulation, hypertension mechanisms, and renal physiology. Its well-defined sequence and high stability make it indispensable for laboratories conducting enzyme kinetics, drug screening assays, and preclinical studies aimed at developing novel therapeutics for cardiovascular and kidney-related disorders, providing a reliable standard for both in vitro and in vivo experimental models.
